ArticleThe Journal of biological chemistry
Real-time identification of two substrate-binding intermediates for the light-driven sodium pump rhodopsin.
Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- The Conformational Switches of a Bacterial Light-Driven Sodium Pump Characterized by Time-Resolved Resonance Raman Spectroscopy.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Mechanistic insights into NaThe Journal of biological chemistry · 2026Article
- A Detailed View on the (Re)isomerization Dynamics in Microbial Rhodopsins Using Complementary Near-UV and IR Readouts.Angewandte Chemie (International ed. in English) · 2025Article
- Direct detection of the chloride release and uptake reactions of Natronomonas pharaonis halorhodopsin.The Journal of biological chemistry · 2024Article
- A subgroup of light-driven sodium pumps with an additional Schiff base counterion.Nature communications · 2024Article
- NaMolecules (Basel, Switzerland) · 2023Review
- KInternational journal of molecular sciences · 2023Article
- Ion-transporting mechanism in microbial rhodopsins: Mini-review relating to the session 5 at the 19th International Conference on Retinal Proteins.Biophysics and physicobiology · 2023Article
- Structural and functional consequences of the H180A mutation of the light-driven sodium pump KR2.Biophysical journal · 2023Article
- Mutations conferring SOScientific reports · 2022Article
- Reisomerization of retinal represents a molecular switch mediating NaThe Journal of biological chemistry · 2022Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane transport proteins undergo critical conformational changes during substrate uptake and release, as the substrate-binding site is believed to switch its accessibility from one side of the membrane to the other. Thus, at least two substrate-binding intermediates should appear during the process, that is, after uptake and before the release of the substrate. However, this view has not been verified for most transporters because of the difficulty in detecting short-lived intermediates. Here, we report real-time identification of these intermediates for the light-driven outward current-generating Na
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.